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SWI/SNF complex subunit SMARCC1 (BRG1-associated factor 155) (SWI/SNF complex 155 kDa subunit) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 1) (SWI3-related protein) (BAF155)

 SMRC1_MOUSE             Reviewed;        1104 AA.
P97496; Q7TS80; Q7TT29;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
04-JAN-2005, sequence version 2.
23-MAY-2018, entry version 166.
RecName: Full=SWI/SNF complex subunit SMARCC1;
AltName: Full=BRG1-associated factor 155;
AltName: Full=SWI/SNF complex 155 kDa subunit;
AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 1;
AltName: Full=SWI3-related protein;
Short=BAF155;
Name=Smarcc1; Synonyms=Baf155, Srg3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J;
PubMed=9151708; DOI=10.1084/jem.185.10.1827;
Jeon S.H., Kang M.G., Kim Y.H., Jin Y.H., Lee C., Chung H.-Y.,
Kwon H., Park S.D., Seong R.H.;
"A new mouse gene, SRG3, related to the SWI3 of Saccharomyces
cerevisiae, is required for apoptosis induced by glucocorticoids in a
thymoma cell line.";
J. Exp. Med. 185:1827-1836(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-892 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION.
PubMed=11604513; DOI=10.1128/MCB.21.22.7787-7795.2001;
Kim J.K., Huh S.-O., Choi H., Lee K.-S., Shin D., Lee C., Nam J.-S.,
Kim H., Chung H., Lee H.W., Park S.D., Seong R.H.;
"Srg3, a mouse homolog of yeast SWI3, is essential for early
embryogenesis and involved in brain development.";
Mol. Cell. Biol. 21:7787-7795(2001).
[4]
FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS
SPECTROMETRY, IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES, AND
DEVELOPMENTAL STAGE.
PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T.,
Wu H., Aebersold R., Graef I.A., Crabtree G.R.;
"An essential switch in subunit composition of a chromatin remodeling
complex during neural development.";
Neuron 55:201-215(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-329, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327; SER-329; SER-572;
SER-775; SER-821 AND SER-824, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
INTERACTION WITH CEBPB.
PubMed=20111005; DOI=10.1038/emboj.2010.3;
Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A.;
"Crosstalk between C/EBPbeta phosphorylation, arginine methylation,
and SWI/SNF/Mediator implies an indexing transcription factor code.";
EMBO J. 29:1105-1115(2010).
[8]
INTERACTION WITH KDM6B.
PubMed=21095589; DOI=10.1016/j.molcel.2010.10.028;
Miller S.A., Mohn S.E., Weinmann A.S.;
"Jmjd3 and UTX play a demethylase-independent role in chromatin
remodeling to regulate T-box family member-dependent gene
expression.";
Mol. Cell 40:594-605(2010).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-345, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[10]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1064, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[11]
REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
PubMed=22952240; DOI=10.1074/jbc.R111.309302;
Euskirchen G., Auerbach R.K., Snyder M.;
"SWI/SNF chromatin-remodeling factors: multiscale analyses and diverse
functions.";
J. Biol. Chem. 287:30897-30905(2012).
[12]
REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
PubMed=26601204; DOI=10.1126/sciadv.1500447;
Kadoch C., Crabtree G.R.;
"Mammalian SWI/SNF chromatin remodeling complexes and cancer:
Mechanistic insights gained from human genomics.";
Sci. Adv. 1:E1500447-E1500447(2015).
-!- FUNCTION: Involved in transcriptional activation and repression of
select genes by chromatin remodeling (alteration of DNA-nucleosome
topology). Component of SWI/SNF chromatin remodeling complexes
that carry out key enzymatic activities, changing chromatin
structure by altering DNA-histone contacts within a nucleosome in
an ATP-dependent manner. May stimulate the ATPase activity of the
catalytic subunit of the complex. Belongs to the neural
progenitors-specific chromatin remodeling complex (npBAF complex)
and the neuron-specific chromatin remodeling complex (nBAF
complex). During neural development a switch from a
stem/progenitor to a postmitotic chromatin remodeling mechanism
occurs as neurons exit the cell cycle and become committed to
their adult state. The transition from proliferating neural
stem/progenitor cells to postmitotic neurons requires a switch in
subunit composition of the npBAF and nBAF complexes. As neural
progenitors exit mitosis and differentiate into neurons, npBAF
complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are
exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B
or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The
npBAF complex is essential for the self-renewal/proliferative
capacity of the multipotent neural stem cells. The nBAF complex
along with CREST plays a role regulating the activity of genes
essential for dendrite growth. {ECO:0000250|UniProtKB:Q92922,
ECO:0000269|PubMed:11604513, ECO:0000269|PubMed:17640523,
ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
-!- SUBUNIT: Component of the multiprotein chromatin-remodeling
complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related
complexes. The canonical complex contains a catalytic subunit
(either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least
SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and
SMARCB1/SNF5/BAF47. Other subunits specific to each of the
complexes may also be present permitting several possible
combinations developmentally and tissue specific (Probable).
Component of the BAF complex, which includes at least actin
(ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1,
ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155,
SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A,
SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF
complex also contains DPF3 (By similarity). Component of neural
progenitors-specific chromatin remodeling complex (npBAF complex)
composed of at least, ARID1A/BAF250A or ARID1B/BAF250B,
SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B,
SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155,
SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and
actin. Component of neuron-specific chromatin remodeling complex
(nBAF complex) composed of at least, ARID1A/BAF250A or
ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523). Component
of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least
composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or
ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B,
perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170,
PBRM1/BAF180, ARID2/BAF200 and actin (PubMed:22952240,
PubMed:26601204). May also interact with the SIN3A histone
deacetylase transcription repressor complex in conjunction with
SMARCA2 and SMARCA4. The minimal complex composed of SMARCC1 and
SMARCA4 seems to be able to associate with cyclin such as CCNE1 or
transcription factors such as KLF1 or GATA1. Interacts with NR3C1
and SMARD1. Interacts with TRIP12; leading to disrupt interaction
between TRIP12 and SMARCE1 and prevent SMARCE1 ubiquitination (By
similarity). Interacts with CEBPB (when not
methylated)(PubMed:20111005). Interacts with KDM6B
(PubMed:21095589). Interacts with MKKS; the interaction takes
place predominantly in the cytoplasm and may modulate SMARCC1
location (By similarity). {ECO:0000250|UniProtKB:P97496,
ECO:0000250|UniProtKB:Q92922, ECO:0000269|PubMed:17640523,
ECO:0000269|PubMed:20111005, ECO:0000269|PubMed:21095589,
ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
-!- INTERACTION:
Q3TKT4:Smarca4; NbExp=7; IntAct=EBI-648047, EBI-1210244;
Q9Z0H3:Smarcb1; NbExp=5; IntAct=EBI-648047, EBI-689365;
Q61466:Smarcd1; NbExp=3; IntAct=EBI-648047, EBI-371529;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm
{ECO:0000250|UniProtKB:Q92922}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P97496-1; Sequence=Displayed;
Name=2;
IsoId=P97496-2; Sequence=VSP_012489;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in adult brain, testis and
thymus.
-!- DEVELOPMENTAL STAGE: Highly expressed in all organs except heart
and liver (E12.5 and E14.5). The level of expression gradually
diminishes as embryos develop, with expression restricted mostly
to the CNS and thymus at E18.5. Expressed ubiquitously throughout
the developing spinal cord, brain and other embryonic tissues at
E10.5-E16.5. {ECO:0000269|PubMed:17640523}.
-!- SIMILARITY: Belongs to the SMARCC family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB42085.1; Type=Frameshift; Positions=5, 32, 48, 563, 565, 679, 682; Evidence={ECO:0000305};
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EMBL; U85614; AAB42085.1; ALT_FRAME; mRNA.
EMBL; BC052423; AAH52423.1; -; mRNA.
EMBL; BC053064; AAH53064.1; -; mRNA.
CCDS; CCDS23561.1; -. [P97496-1]
PIR; T30967; T30967.
RefSeq; NP_033237.2; NM_009211.2. [P97496-1]
UniGene; Mm.85410; -.
ProteinModelPortal; P97496; -.
SMR; P97496; -.
BioGrid; 203338; 35.
CORUM; P97496; -.
DIP; DIP-39986N; -.
IntAct; P97496; 36.
MINT; P97496; -.
STRING; 10090.ENSMUSP00000086094; -.
iPTMnet; P97496; -.
PhosphoSitePlus; P97496; -.
SwissPalm; P97496; -.
MaxQB; P97496; -.
PaxDb; P97496; -.
PeptideAtlas; P97496; -.
PRIDE; P97496; -.
Ensembl; ENSMUST00000088716; ENSMUSP00000086094; ENSMUSG00000032481. [P97496-1]
Ensembl; ENSMUST00000197984; ENSMUSP00000142611; ENSMUSG00000032481. [P97496-2]
GeneID; 20588; -.
KEGG; mmu:20588; -.
UCSC; uc009rto.1; mouse. [P97496-2]
UCSC; uc009rtp.1; mouse. [P97496-1]
CTD; 6599; -.
MGI; MGI:1203524; Smarcc1.
eggNOG; KOG1279; Eukaryota.
eggNOG; COG5259; LUCA.
GeneTree; ENSGT00390000018166; -.
HOGENOM; HOG000047736; -.
HOVERGEN; HBG054849; -.
InParanoid; P97496; -.
KO; K11649; -.
OMA; YKKYVHA; -.
OrthoDB; EOG091G06AJ; -.
PhylomeDB; P97496; -.
TreeFam; TF314710; -.
Reactome; R-MMU-3214858; RMTs methylate histone arginines.
Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
ChiTaRS; Smarcc1; mouse.
PRO; PR:P97496; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032481; -.
ExpressionAtlas; P97496; baseline and differential.
Genevisible; P97496; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0071565; C:nBAF complex; IDA:UniProtKB.
GO; GO:0071564; C:npBAF complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016514; C:SWI/SNF complex; IDA:MGI.
GO; GO:0001741; C:XY body; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IEA:InterPro.
GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
GO; GO:0006323; P:DNA packaging; TAS:MGI.
GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:MGI.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0006337; P:nucleosome disassembly; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0030850; P:prostate gland development; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00024; CHROMO; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR030087; BAF155.
InterPro; IPR036420; BRCT_dom_sf.
InterPro; IPR000953; Chromo/chromo_shadow_dom.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR017884; SANT_dom.
InterPro; IPR032451; SMARCC_C.
InterPro; IPR032450; SMARCC_N.
InterPro; IPR007526; SWIRM.
InterPro; IPR032448; SWIRM-assoc.
InterPro; IPR036388; WH-like_DNA-bd_sf.
PANTHER; PTHR12802:SF9; PTHR12802:SF9; 1.
Pfam; PF00249; Myb_DNA-binding; 1.
Pfam; PF04433; SWIRM; 1.
Pfam; PF16495; SWIRM-assoc_1; 1.
Pfam; PF16496; SWIRM-assoc_2; 1.
Pfam; PF16498; SWIRM-assoc_3; 1.
SMART; SM00298; CHROMO; 1.
SMART; SM00717; SANT; 1.
SUPFAM; SSF46689; SSF46689; 2.
SUPFAM; SSF52113; SSF52113; 2.
PROSITE; PS51293; SANT; 1.
PROSITE; PS50934; SWIRM; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Chromatin regulator; Coiled coil;
Complete proteome; Cytoplasm; Isopeptide bond; Methylation;
Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 1104 SWI/SNF complex subunit SMARCC1.
/FTId=PRO_0000197116.
DOMAIN 448 545 SWIRM. {ECO:0000255|PROSITE-
ProRule:PRU00247}.
DOMAIN 617 668 SANT. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
COILED 909 945 {ECO:0000255}.
COMPBIAS 326 333 Poly-Pro.
COMPBIAS 768 862 Glu-rich.
COMPBIAS 866 877 Poly-Ala.
COMPBIAS 977 1104 Pro-rich.
MOD_RES 309 309 Phosphoserine.
{ECO:0000250|UniProtKB:Q92922}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 334 334 Phosphothreonine.
{ECO:0000250|UniProtKB:Q92922}.
MOD_RES 344 344 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q92922}.
MOD_RES 345 345 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 349 349 Phosphoserine.
{ECO:0000250|UniProtKB:Q92922}.
MOD_RES 353 353 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q92922}.
MOD_RES 356 356 Phosphoserine.
{ECO:0000250|UniProtKB:Q92922}.
MOD_RES 358 358 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q92922}.
MOD_RES 397 397 Phosphothreonine.
{ECO:0000250|UniProtKB:Q92922}.
MOD_RES 572 572 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 775 775 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 821 821 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 824 824 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 947 947 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q92922}.
MOD_RES 1064 1064 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
CROSSLNK 178 178 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92922}.
CROSSLNK 358 358 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q92922}.
CROSSLNK 591 591 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92922}.
CROSSLNK 738 738 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92922}.
CROSSLNK 795 795 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92922}.
CROSSLNK 828 828 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92922}.
CROSSLNK 855 855 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92922}.
VAR_SEQ 1074 1104 YPPPPQQQQPPPPADGVPPPPAPGPPASATP -> CK (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012489.
CONFLICT 132 132 G -> S (in Ref. 1; AAB42085).
{ECO:0000305}.
CONFLICT 468 468 R -> G (in Ref. 1; AAB42085).
{ECO:0000305}.
CONFLICT 498 498 R -> C (in Ref. 1; AAB42085).
{ECO:0000305}.
CONFLICT 512 512 R -> L (in Ref. 1; AAB42085).
{ECO:0000305}.
CONFLICT 883 883 L -> P (in Ref. 1; AAB42085).
{ECO:0000305}.
CONFLICT 891 891 I -> K (in Ref. 2; AAH53064).
{ECO:0000305}.
CONFLICT 952 952 R -> L (in Ref. 2; AAH52423).
{ECO:0000305}.
CONFLICT 984 984 A -> R (in Ref. 1; AAB42085).
{ECO:0000305}.
SEQUENCE 1104 AA; 122890 MW; 9030545104B90CAF CRC64;
MAATAGGGPG AAAGAVGAGG AAAASGLAVY RRKDGGPASK FWESPDTVSQ LDSVRVWLGK
HYKKYVHADA PTNKTLAGLV VQLLQFQEDA FGKHVTNPAF TKLPAKCFMD FKAGGTLCHI
LGAAYKYKNE QGWRRFDLQN PSRMDRNVEM FMNIEKTLVQ NNCLTRPNIY LIPDIDLKLA
NKLKDIIKRH QGTFTDEKSK ASHHIYPYPS SQEDEEWLRP VMRRDKQVLV HWGFYPDSYD
TWVHSNDVDA EIEDAPIPEK PWKVHVKWIL DTDVFNEWMN EEDYEVDENR KPVSFRQRIS
TKNEEPVRSP ERRDRKASAN SRKRKPSPSP PPPTATESRK KSGKKGQASL YGKRRSQKEE
DEQEDLTKDM EDPTPVPNIE EVVLPKNVNP KKDSENTPVK GGTVADLDEQ DEEAVTTGGK
EDEDPSKGDP SRSVDPGEDN VTEQTNHIII PSYASWFDYN CIHVIERRAL PEFFNGKNKS
KTPEIYLAYR NFMIDTYRLN PQEYLTSTAC RRNLTGDVCA VMRVHAFLEQ WGLVNYQVDP
ESRPMAMGPP PTPHFNVLAD TPSGLVPLHL RSPQVPAAQQ MLNFPEKNKE KPIDLQNFGL
RTDIYSKKTL AKSKGASAGR EWTEQETLLL LEALEMYKDD WNKVSEHVGS RTQDECILHF
LRLPIEDPYL ENSDASLGPL AYQPVPFSQS GNPVMSTVAF LASVVDPRVA SAAAKAALEE
FSRVREEVPL ELVEAHVKKV QEAARASGKV DPTYGLESSC IAGTGPDEPE KLEGSEEEKM
ETDPDGQQPE KAENKVENES DEGDKIQDRE NEKNTEKEQD SDVSEDVKPE EKENEENKEL
TDTCKERESD AGKKKVEHEI SEGNVATAAA AALASAATKA KHLAAVEERK IKSLVALLVE
TQMKKLEIKL RHFEELETIM DREKEALEQQ RQQLLTERQN FHMEQLKYAE LRARQQMEQQ
QQHGQTPQQA HQHTGGPGMA PLGATGHPGM MPHQQPPPYP LMHHQMPPPH PPQPGQIPGP
GSMMPGQPMP GRMIPAVAAN IHPTGSGPTP PGMPPMPGNI LGPRVPLTAP NGMYPPPPQQ
QQPPPPADGV PPPPAPGPPA SATP


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